Neutrophil-activating protein mediates adhesion of Helicobacter pylori to sulfated carbohydrates on high-molecular-weight salivary mucin.
The in vitro binding of surface-exposed material and outer membrane proteins of Helicobacter pylori to high-molecular-weight salivary mucin was studied. We identified a 16-kDa surface protein which adhered to high-molecular-weight salivary mucin. This protein binds specifically to sulfated oligosaccharide structures such as sulfo-Lewis a, sulfogalactose and sulfo-N-acetyl-glucosamine on mucin. Sequence analysis of the protein proved that it was identical to the N-terminal amino acid sequence of neutrophil-activating protein. Moreover, this adhesin was able to bind to Lewis x blood group antigen.
Namavar
F
F
Department of Medical Microbiology, Medical School, Vrije Universiteit, Amsterdam, The Netherlands. F.Namavar.mm@med.vu.nl
Sparrius
M
M
Veerman
E C
EC
Appelmelk
B J
BJ
Vandenbroucke-Grauls
C M
CM
D000595:Amino Acid Sequence; D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000502:physiology*; D018821:CD18 Antigens / Q000502:physiology; D016480:Helicobacter pylori / Q000502:physiology*; D006801:Humans; D007983:Lewis Blood Group Antigens / Q000378:metabolism; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009077:Mucins / Q000378:metabolism*; D009844:Oligosaccharides / Q000378:metabolism; D012463:Saliva / Q000382:microbiology*
D001426:Bacterial Proteins; D018821:CD18 Antigens; D007983:Lewis Blood Group Antigens; D009077:Mucins; D009844:Oligosaccharides; C092412:neutrophil-activating protein A, Helicobacter pylori